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Ras-like GTP-binding protein Rho1

 RHO1_DROME              Reviewed;         192 AA.
P48148; A4UZI6; Q0E958; Q9V3J0;
01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 1.
25-OCT-2017, entry version 168.
RecName: Full=Ras-like GTP-binding protein Rho1;
Flags: Precursor;
Name=Rho1 {ECO:0000312|FlyBase:FBgn0014020};
ORFNames=CG8416 {ECO:0000312|FlyBase:FBgn0014020};
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
PubMed=7835340;
Hariharan I.K., Hu K.-Q., Asha H., Quintanilla A., Ezzell R.M.,
Settleman J.;
"Characterization of rho GTPase family homologues in Drosophila
melanogaster: overexpressing Rho1 in retinal cells causes a late
developmental defect.";
EMBO J. 14:292-302(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, INTERACTION WITH
CAPU, AND DISRUPTION PHENOTYPE.
PubMed=10556060;
Magie C.R., Meyer M.R., Gorsuch M.S., Parkhurst S.M.;
"Mutations in the Rho1 small GTPase disrupt morphogenesis and
segmentation during early Drosophila development.";
Development 126:5353-5364(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Head;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
Celniker S.E.;
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[7]
FUNCTION, AND INTERACTION WITH PKN.
PubMed=10323867; DOI=10.1101/gad.13.9.1168;
Lu Y., Settleman J.;
"The Drosophila Pkn protein kinase is a Rho/Rac effector target
required for dorsal closure during embryogenesis.";
Genes Dev. 13:1168-1180(1999).
[8]
INTERACTION WITH PKN.
PubMed=17507675; DOI=10.1534/genetics.107.072967;
Betson M., Settleman J.;
"A rho-binding protein kinase C-like activity is required for the
function of protein kinase N in Drosophila development.";
Genetics 176:2201-2212(2007).
[9]
FUNCTION, SUBUNIT, TISSUE SPECIFICITY, AND MUTAGENESIS OF
27-LYS--GLN-29; PHE-39 AND 51-LYS--GLU-54.
PubMed=25739458; DOI=10.1091/mbc.E14-08-1266;
Verboon J.M., Rahe T.K., Rodriguez-Mesa E., Parkhurst S.M.;
"Wash functions downstream of Rho1 GTPase in a subset of Drosophila
immune cell developmental migrations.";
Mol. Biol. Cell 26:1665-1674(2015).
-!- FUNCTION: Has a role in regulating actin cytoskeletal
organization: required during early development for proper
execution of morphogenetic movements of individual cells and
groups of cells important for the formation of the embryonic body
plan (PubMed:10556060, PubMed:25739458). Plays a role in
regulating dorsal closure during embryogenesis (PubMed:10556060,
PubMed:10323867). During embryogenesis, acts upstream of wash to
regulate the developmental migration of tail hemocytes anteriorly
along the ventral midline (PubMed:25739458). May have a role in
eye development (PubMed:7835340). {ECO:0000269|PubMed:10323867,
ECO:0000269|PubMed:10556060, ECO:0000269|PubMed:25739458,
ECO:0000269|PubMed:7835340}.
-!- SUBUNIT: Interacts with capu (PubMed:10556060). Interacts (via REM
repeats) with Pkn (via N-terminus) (PubMed:10323867,
PubMed:17507675). Interacts (via N-terminus) with wash (via N-
terminus) (PubMed:25739458). {ECO:0000269|PubMed:10323867,
ECO:0000269|PubMed:10556060, ECO:0000269|PubMed:17507675}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor
{ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm,
cytoskeleton.
-!- TISSUE SPECIFICITY: Expressed in hemocytes (at protein level).
{ECO:0000269|PubMed:25739458}.
-!- DISRUPTION PHENOTYPE: Embryonic lethal. Embryos exhibit severe
defects in head involution and imperfect dorsal closure. During
head involution, the head structures fail to internalize resulting
in holes in the dorsal anterior region of the cuticle. The
disruption in the dorsal surface stretches the ventral surface,
causing the cuticle to bow. {ECO:0000269|PubMed:10556060}.
-!- SIMILARITY: Belongs to the small GTPase superfamily. Rho family.
{ECO:0000305}.
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EMBL; L38311; AAA67042.1; -; mRNA.
EMBL; AF177871; AAF01183.1; -; Genomic_DNA.
EMBL; AF177872; AAF01184.1; -; mRNA.
EMBL; AF177873; AAF01185.1; -; mRNA.
EMBL; AF177874; AAF01186.1; -; mRNA.
EMBL; AE013599; AAM70944.1; -; Genomic_DNA.
EMBL; AE013599; AAM70945.1; -; Genomic_DNA.
EMBL; AE013599; AAM70946.1; -; Genomic_DNA.
EMBL; AE013599; AAS64843.1; -; Genomic_DNA.
EMBL; AE013599; AAS64844.1; -; Genomic_DNA.
EMBL; AY119536; AAM50190.1; -; mRNA.
EMBL; BT010085; AAQ22554.1; -; mRNA.
PIR; S54294; S54294.
RefSeq; NP_477098.1; NM_057750.4.
RefSeq; NP_599135.1; NM_134308.3.
RefSeq; NP_599136.1; NM_134309.2.
RefSeq; NP_725524.1; NM_166139.3.
RefSeq; NP_995849.1; NM_206127.2.
RefSeq; NP_995850.1; NM_206128.2.
UniGene; Dm.644; -.
ProteinModelPortal; P48148; -.
SMR; P48148; -.
BioGrid; 62500; 88.
DIP; DIP-22676N; -.
IntAct; P48148; 1.
MINT; MINT-312636; -.
STRING; 7227.FBpp0086354; -.
PaxDb; P48148; -.
PRIDE; P48148; -.
EnsemblMetazoa; FBtr0087211; FBpp0086353; FBgn0014020.
EnsemblMetazoa; FBtr0087212; FBpp0086354; FBgn0014020.
EnsemblMetazoa; FBtr0087213; FBpp0086355; FBgn0014020.
EnsemblMetazoa; FBtr0087214; FBpp0086356; FBgn0014020.
EnsemblMetazoa; FBtr0087216; FBpp0089129; FBgn0014020.
EnsemblMetazoa; FBtr0087217; FBpp0089130; FBgn0014020.
GeneID; 36775; -.
KEGG; dme:Dmel_CG8416; -.
UCSC; CG8416-RC; d. melanogaster.
CTD; 36775; -.
FlyBase; FBgn0014020; Rho1.
eggNOG; KOG0393; Eukaryota.
eggNOG; COG1100; LUCA.
GeneTree; ENSGT00760000119020; -.
InParanoid; P48148; -.
KO; K04513; -.
OMA; QKIGARH; -.
OrthoDB; EOG091G0QVS; -.
PhylomeDB; P48148; -.
Reactome; R-DME-114604; GPVI-mediated activation cascade.
Reactome; R-DME-193634; Axonal growth inhibition (RHOA activation).
Reactome; R-DME-194840; Rho GTPase cycle.
Reactome; R-DME-198203; PI3K/AKT activation.
Reactome; R-DME-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
Reactome; R-DME-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-DME-3928662; EPHB-mediated forward signaling.
Reactome; R-DME-3928663; EPHA-mediated growth cone collapse.
Reactome; R-DME-4086400; PCP/CE pathway.
Reactome; R-DME-416482; G alpha (12/13) signalling events.
Reactome; R-DME-416572; Sema4D induced cell migration and growth-cone collapse.
Reactome; R-DME-4420097; VEGFA-VEGFR2 Pathway.
Reactome; R-DME-5625740; RHO GTPases activate PKNs.
Reactome; R-DME-5625900; RHO GTPases activate CIT.
Reactome; R-DME-5627117; RHO GTPases Activate ROCKs.
Reactome; R-DME-5663220; RHO GTPases Activate Formins.
Reactome; R-DME-5666185; RHO GTPases Activate Rhotekin and Rhophilins.
Reactome; R-DME-5689896; Ovarian tumor domain proteases.
Reactome; R-DME-6785631; ERBB2 Regulates Cell Motility.
Reactome; R-DME-6798695; Neutrophil degranulation.
Reactome; R-DME-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
ChiTaRS; Rho1; fly.
GenomeRNAi; 36775; -.
PRO; PR:P48148; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0014020; -.
Genevisible; P48148; DM.
GO; GO:0045179; C:apical cortex; IDA:FlyBase.
GO; GO:0005938; C:cell cortex; IDA:FlyBase.
GO; GO:0070451; C:cell hair; IDA:FlyBase.
GO; GO:0044291; C:cell-cell contact zone; IDA:FlyBase.
GO; GO:0005737; C:cytoplasm; IDA:FlyBase.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:FlyBase.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0003924; F:GTPase activity; IDA:FlyBase.
GO; GO:0019900; F:kinase binding; IPI:FlyBase.
GO; GO:0030036; P:actin cytoskeleton organization; IMP:FlyBase.
GO; GO:0031532; P:actin cytoskeleton reorganization; IDA:FlyBase.
GO; GO:0051017; P:actin filament bundle assembly; IMP:FlyBase.
GO; GO:0007015; P:actin filament organization; IMP:FlyBase.
GO; GO:0070252; P:actin-mediated cell contraction; IGI:FlyBase.
GO; GO:0034334; P:adherens junction maintenance; IMP:FlyBase.
GO; GO:0034332; P:adherens junction organization; IMP:UniProtKB.
GO; GO:0007411; P:axon guidance; IMP:FlyBase.
GO; GO:0007298; P:border follicle cell migration; IMP:FlyBase.
GO; GO:0090254; P:cell elongation involved in imaginal disc-derived wing morphogenesis; IMP:FlyBase.
GO; GO:0034613; P:cellular protein localization; IMP:FlyBase.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:FlyBase.
GO; GO:0007349; P:cellularization; IMP:FlyBase.
GO; GO:0001745; P:compound eye morphogenesis; IGI:FlyBase.
GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:FlyBase.
GO; GO:0042335; P:cuticle development; IGI:UniProtKB.
GO; GO:0048813; P:dendrite morphogenesis; TAS:FlyBase.
GO; GO:0070593; P:dendrite self-avoidance; IGI:FlyBase.
GO; GO:0007368; P:determination of left/right symmetry; IMP:FlyBase.
GO; GO:0007391; P:dorsal closure; IMP:UniProtKB.
GO; GO:0046663; P:dorsal closure, leading edge cell differentiation; IMP:FlyBase.
GO; GO:0007395; P:dorsal closure, spreading of leading edge cells; IMP:FlyBase.
GO; GO:0032456; P:endocytic recycling; IMP:FlyBase.
GO; GO:0006897; P:endocytosis; IMP:FlyBase.
GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; IGI:FlyBase.
GO; GO:0042249; P:establishment of planar polarity of embryonic epithelium; IMP:FlyBase.
GO; GO:0045184; P:establishment of protein localization; IMP:FlyBase.
GO; GO:0030950; P:establishment or maintenance of actin cytoskeleton polarity; IMP:FlyBase.
GO; GO:0010004; P:gastrulation involving germ band extension; IMP:FlyBase.
GO; GO:0007377; P:germ-band extension; IMP:FlyBase.
GO; GO:0008347; P:glial cell migration; IMP:FlyBase.
GO; GO:0035099; P:hemocyte migration; IMP:FlyBase.
GO; GO:0007480; P:imaginal disc-derived leg morphogenesis; IMP:FlyBase.
GO; GO:0035317; P:imaginal disc-derived wing hair organization; IMP:FlyBase.
GO; GO:0035149; P:lumen formation, open tracheal system; IMP:FlyBase.
GO; GO:0045199; P:maintenance of epithelial cell apical/basal polarity; IMP:FlyBase.
GO; GO:0035006; P:melanization defense response; IMP:FlyBase.
GO; GO:1903475; P:mitotic actomyosin contractile ring assembly; IMP:FlyBase.
GO; GO:0000281; P:mitotic cytokinesis; IMP:FlyBase.
GO; GO:0008045; P:motor neuron axon guidance; IMP:FlyBase.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IMP:FlyBase.
GO; GO:0007405; P:neuroblast proliferation; IMP:FlyBase.
GO; GO:0048812; P:neuron projection morphogenesis; IMP:FlyBase.
GO; GO:0007424; P:open tracheal system development; IMP:FlyBase.
GO; GO:0007422; P:peripheral nervous system development; IMP:FlyBase.
GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; IDA:UniProtKB.
GO; GO:0090303; P:positive regulation of wound healing; IDA:FlyBase.
GO; GO:0007374; P:posterior midgut invagination; IMP:FlyBase.
GO; GO:0090251; P:protein localization involved in establishment of planar polarity; IMP:FlyBase.
GO; GO:0071896; P:protein localization to adherens junction; IMP:FlyBase.
GO; GO:0030589; P:pseudocleavage involved in syncytial blastoderm formation; IMP:FlyBase.
GO; GO:0050770; P:regulation of axonogenesis; IGI:FlyBase.
GO; GO:0030334; P:regulation of cell migration; IMP:FlyBase.
GO; GO:0051493; P:regulation of cytoskeleton organization; IDA:FlyBase.
GO; GO:0016476; P:regulation of embryonic cell shape; IMP:FlyBase.
GO; GO:0051489; P:regulation of filopodium assembly; IMP:FlyBase.
GO; GO:1904059; P:regulation of locomotor rhythm; IMP:FlyBase.
GO; GO:0035298; P:regulation of Malpighian tubule size; IMP:FlyBase.
GO; GO:1901739; P:regulation of myoblast fusion; IGI:FlyBase.
GO; GO:0035159; P:regulation of tube length, open tracheal system; IMP:FlyBase.
GO; GO:0007435; P:salivary gland morphogenesis; IMP:FlyBase.
GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
GO; GO:0035277; P:spiracle morphogenesis, open tracheal system; IMP:FlyBase.
GO; GO:0007370; P:ventral furrow formation; IMP:FlyBase.
GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
GO; GO:0016055; P:Wnt signaling pathway; NAS:FlyBase.
GO; GO:0042060; P:wound healing; IMP:FlyBase.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR005225; Small_GTP-bd_dom.
InterPro; IPR001806; Small_GTPase.
InterPro; IPR003578; Small_GTPase_Rho.
Pfam; PF00071; Ras; 1.
SUPFAM; SSF52540; SSF52540; 1.
TIGRFAMs; TIGR00231; small_GTP; 1.
PROSITE; PS51420; RHO; 1.
1: Evidence at protein level;
Actin-binding; Cell membrane; Complete proteome; Cytoplasm;
Cytoskeleton; Developmental protein; GTP-binding; Lipoprotein;
Membrane; Methylation; Nucleotide-binding; Prenylation;
Reference proteome; Sensory transduction; Vision.
CHAIN 1 189 Ras-like GTP-binding protein Rho1.
/FTId=PRO_0000198885.
PROPEP 190 192 Removed in mature form. {ECO:0000250}.
/FTId=PRO_0000281238.
NP_BIND 12 19 GTP. {ECO:0000250}.
NP_BIND 59 63 GTP. {ECO:0000250}.
NP_BIND 117 120 GTP. {ECO:0000250}.
MOTIF 34 42 Effector region. {ECO:0000255}.
MOD_RES 189 189 Cysteine methyl ester. {ECO:0000250}.
LIPID 189 189 S-geranylgeranyl cysteine. {ECO:0000250}.
MUTAGEN 27 29 KDQ->AAA: Reduces binding to wash.
Reduces the number of hemocytes migrating
anteriorly from the tail during
embryogenesis.
{ECO:0000269|PubMed:25739458}.
MUTAGEN 39 39 F->V: No effect on binding to wash and no
effect on tail hemocyte developmental
migration from the tail.
{ECO:0000269|PubMed:25739458}.
MUTAGEN 51 54 KQVE->AAAA: No effect on binding to wash.
{ECO:0000269|PubMed:25739458}.
SEQUENCE 192 AA; 21723 MW; B89C7D884E1743CF CRC64;
MTTIRKKLVI VGDGACGKTC LLIVFSKDQF PEVYVPTVFE NYVADIEVDG KQVELALWDT
AGQEDYDRLR PLSYPDTDVI LMCFSVDSPD SLENIPEKWT PEVKHFCPNV PIILVGNKKD
LRNDPNTIRD LAKMKQEPVK PQEGRAMAEK INAFAYLECS AKSKEGVRDV FETATRAALQ
VKKRKKTRCL LL


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18-003-44208 Insulin-like growth factor 2 mRNA-binding protein 1 - IGF2 mRNA-binding protein 1; IGF-II mRNA-binding protein 1; IMP-1; Coding region determinant-binding protein; CRD-BP; VICKZ family member 1 Polycl 0.05 mg Aff Pur
EIAAB31031 DDXBP1,DEAD_H box-binding protein 1,E3 SUMO-protein ligase PIAS1,GBP,Gu-binding protein,Homo sapiens,Human,PIAS1,Protein inhibitor of activated STAT protein 1,RNA helicase II-binding protein
EIAAB34014 Rat,Rattus norvegicus,Rbm30,Rbm4b,RNA-binding motif protein 30,RNA-binding motif protein 4B,RNA-binding protein 30,RNA-binding protein 4B,Zinc-responsive protein ZD7
EIAAB33940 DXS8237E,G patch domain-containing protein 9,GPATC9,GPATCH9,Homo sapiens,Human,KIAA0122,RBM10,RNA-binding motif protein 10,RNA-binding protein 10,RNA-binding protein S1-1,S1-1
EIAAB10707 Damage-specific DNA-binding protein 1,DDB p127 subunit,DDB1,DDBa,DNA damage-binding protein 1,DNA damage-binding protein a,HBV X-associated protein 1,Homo sapiens,Human,UV-damaged DNA-binding factor,U
U1257h CLIA DEF3,Homo sapiens,Human,Lung cancer antigen NY-LU-12,Protein G16,RBM6,RNA-binding motif protein 6,RNA-binding protein 6,RNA-binding protein DEF-3 96T
E1257h ELISA kit DEF3,Homo sapiens,Human,Lung cancer antigen NY-LU-12,Protein G16,RBM6,RNA-binding motif protein 6,RNA-binding protein 6,RNA-binding protein DEF-3 96T
EIAAB45443 AIE-75-binding protein,AIEBP,Homo sapiens,Human,MCC2,MCC-2,USH1C-binding protein 1,USHBP1,Usher syndrome type-1C protein-binding protein 1
E1257h ELISA DEF3,Homo sapiens,Human,Lung cancer antigen NY-LU-12,Protein G16,RBM6,RNA-binding motif protein 6,RNA-binding protein 6,RNA-binding protein DEF-3 96T
EIAAB47038 Hivep3,Human immunodeficiency virus type I enhancer-binding protein 3 homolog,Kappa-B and V(D)J recombination signal sequences-binding protein,Kappa-binding protein 1,KB-binding and regognition compon


 

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